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TitleHIV Envelope Glycoform Heterogeneity and Localized Diversity Govern the Initiation and Maturation of a V2 Apex Broadly Neutralizing Antibody Lineage.
Journal, issue, pagesImmunity, Vol. 47, Issue 5, Page 990-1003.e9, Year 2017
Publish dateNov 21, 2017
AuthorsElise Landais / Ben Murrell / Bryan Briney / Sasha Murrell / Kimmo Rantalainen / Zachary T Berndsen / Alejandra Ramos / Lalinda Wickramasinghe / Melissa Laird Smith / Kemal Eren / Natalia de Val / Mengyu Wu / Audrey Cappelletti / Jeffrey Umotoy / Yolanda Lie / Terri Wrin / Paul Algate / Po-Ying Chan-Hui / Etienne Karita / / / Andrew B Ward / Ian A Wilson / Dennis R Burton / Davey Smith / Sergei L Kosakovsky Pond / Pascal Poignard /
PubMed AbstractUnderstanding how broadly neutralizing antibodies (bnAbs) to HIV envelope (Env) develop during natural infection can help guide the rational design of an HIV vaccine. Here, we described a bnAb ...Understanding how broadly neutralizing antibodies (bnAbs) to HIV envelope (Env) develop during natural infection can help guide the rational design of an HIV vaccine. Here, we described a bnAb lineage targeting the Env V2 apex and the Ab-Env co-evolution that led to development of neutralization breadth. The lineage Abs bore an anionic heavy chain complementarity-determining region 3 (CDRH3) of 25 amino acids, among the shortest known for this class of Abs, and achieved breadth with only 10% nucleotide somatic hypermutation and no insertions or deletions. The data suggested a role for Env glycoform heterogeneity in the activation of the lineage germline B cell. Finally, we showed that localized diversity at key V2 epitope residues drove bnAb maturation toward breadth, mirroring the Env evolution pattern described for another donor who developed V2-apex targeting bnAbs. Overall, these findings suggest potential strategies for vaccine approaches based on germline-targeting and serial immunogen design.
External linksImmunity / PubMed:29166592 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.1 - 27.0 Å
Structure data

EMDB-7089:
HIV-1 Envelope SOSIP trimer clone PC64M4c054 in complex with autologous PCT64-13C Fab at 13.2 A resolution
Method: EM (single particle) / Resolution: 13.2 Å

EMDB-7104:
HIV-1 Envelope Glycoprotein clone PC64M4c054 SOSIP
Method: EM (single particle) / Resolution: 25.6 Å

EMDB-7105:
HIV-1 Envelope Glycoprotein clone PC64M7c022 SOSIP.664
Method: EM (single particle) / Resolution: 26.0 Å

EMDB-7106:
HIV-1 Envelope Glycoprotein clone PC64M18c043 SOSIP.664
Method: EM (single particle) / Resolution: 24.0 Å

EMDB-7107:
HIV-1 Envelope Glycoprotein clone PC64M4c054 SOSIP in complex with PGV04 Fab
Method: EM (single particle) / Resolution: 27.0 Å

EMDB-7108:
HIV-1 Envelope Glycoprotein clone PC64M18c043 SOSIP.664
Method: EM (single particle) / Resolution: 26.0 Å

PDB-5feh:
Crystal structure of PCT64_35B, a broadly neutralizing anti-HIV antibody
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • Human immunodeficiency virus 1
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / HIV / broadly neutralizing antibody / V1/V2

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